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JJ Liang, L Fu; Conformational Change, Destabilization and Insolubilization of Human Cataract C-Crystallin T5P Mutant . Invest. Ophthalmol. Vis. Sci. 2002;43(13):4656.
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© ARVO (1962-2015); The Authors (2016-present)
Purpose: To study the effects of cataract gene T5P mutation on the biophysical properties of the human γC-crystallin. Methods: Human lens γC-crystallin and T5P mutant were cloned, and conformational change was studied by circular dichroism (CD) and fluorescence measurements, and conformational stability was determined by thermal unfolding probed by Trp fluorescence and time-dependent light scattering. Results: Decreased solubility for T5P mutant was first observed during overexpression. Purified T5P mutant showed decreases in both far and near-UV CD signals, and unfolded and aggregated at lower temperature than the wild-type γC-crystallin did. Conclusion: The T5P mutation obviously changed conformation, a partial unfolding or imperfect folding, and decreased conformational stability.
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